Only selected light chains combine with a given heavy chain to confer specificity for a model glycopeptide antigen

Journal of Immunology

Volumn 160, Issue 9, 1998, Pages 4406-4417

  Czerwinski, Marcin ^a   Siemaszko, Dorota ^a   Siegel, Don L ^b   Spitalnik, Steven L ^b  

^a INSTITUTE OF IMMUNOLOGY AND EXPERIMENTAL THERAPY   (Poland)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; COMPLEMENTARY DNA; GLYCOPEPTIDE; GLYCOPHORIN A; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; MONOCLONAL ANTIBODY;

ANIMAL TISSUE; ARTICLE; BACTERIOPHAGE; BINDING AFFINITY; BINDING SITE; CHIMERA; ENZYME LINKED IMMUNOSORBENT ASSAY; GENE; HUMAN; HUMAN CELL; HUMORAL IMMUNITY; HYBRIDOMA; IMMUNOBLOTTING; MALE; MODEL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODY SPECIFICITY; BASE SEQUENCE; GENE LIBRARY; GLYCOPEPTIDES; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN LIGHT CHAINS; MICE; MNSS BLOOD-GROUP SYSTEM; MOLECULAR SEQUENCE DATA; SEQUENCE ANALYSIS;

EID: 0032080665     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (78)

1. Barbas, C. F., T. A. Collet, W. Amberg, P. Roben, J. M. Binley, D. Hoekstra, D. Cababa, T. M. Jones, R. A. Williamson, G. R. Pilkington, N. L. Haigwood, E. Cabezas, A. C. Satterthwait, I. Sanz, and D. R. Burton. 1993. Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries. J. Mol. Biol. 230:812.
2. L gene segments in the specific binding of antibody to Z-DNA analyzed in recombinant single chain Fv molecules. J. Immunol. 150:469.
3. Portolano, S., G. D. Chazenbalk, J. S. Hutchison, S. M. McLachlan, and B. Rapoport. 1992. Lack of promiscuity in autoantigen-specific H and L chain combinations as revealed by human H and L chain "roulette." J. Immunol. 150: 880.
4. Matsuura, H., T. Greene, and S. Hakomori. 1989. An α-N-acetylgalactosaminylation at the threonine residue of a defined peptide sequence creates the oncofetal peptide epitope in human fibronectin. J. Biol. Chem. 264:10472.
5. Zheng, M., M. Gobbo, L. Blondi, F. Filira, S. Hakomori, and R. Rocchi. 1994. Synthetic immunochemistry of glycohexapeptide analogues characteristic of oncofetal fibronectin: solid-phase synthesis and antigenic activity. Int. J. Peptide Protein Res. 43:230.
6. Hanisch, F. G., T. Stadie, and K. Bosslet. 1995. Monoclonal antibody BW835 defines a site-specific Thomsen-Friedenreich disaccharide linked to threonine within the VTSA motif of MUC1 tandem. Cancer Res. 55:4036.
7. Huang, D. H., K. K. Johe, S. Seifter, and O. O. Blumenfeld. 1991. Biochemistry and molecular biology of MNSs blood group antigens. Balliere Clin. Haematol. 4:821.
8. Chasis, J. A., and N. Mohandas. 1992. Red blood cell glycophorins. Blood 80: 1869.
9. Tomita, M., and V. T. Marchesi. 1975. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc. Natl. Acad. Sci. USA 72:2964.
10. Wasniowska, K., Z. Drzeniek, and E. Lisowska. 1977. The amino acids of M and N blood group glycopeptides are different. Biochem. Biophys. Res. Commun. 76:385.
11. Blumenfeld, O. O., and A.M. Adamany. 1978. Structural polymorphism within the amino-terminal region of MM, NN, and MN glycoproteins (glycophorins) of the human erythrocyte membrane. Proc. Natl. Acad. Sci. USA 75:2727.
12. Lisowska, E., and K. Wasniowska. 1978. Immunochemical characterization of cyanogen bromide degradation products of M and N blood-group glycopeptides. Eur. J. Biochem. 88:247.
13. Dahr, W., G. Uhlenbruck, E. Janssen, and R. Schmalisch. 1977. Different N-terminal amino acids in the MN-glycoprotein from MM and NN erythrocytes. Hum. Genet. 35:335.
14. Bigbee, W. L., M. Vanderlaan, S. S. N. Fong, and R. H. Jensen. 1983. Monoclonal antibodies specific for the M and N forms of human glycophorin A. Mol. Immunol. 20:1353.
15. v type chimpanzee erythrocytes. J. Immunol. 133:3149.
16. Lisowska, E., L. Messeter, M. Duk, M. Czerwinski, and A. Lundblad. 1987. A monoclonal anti-glycophorin A antibody recognizing the blood group M determinant: studies on the subspecificity. Mol. Immunol. 24:605.
17. Jaskiewicz, E., E. Lisowska, and A. Lundblad. 1990. The role of carbohydrate in the blood group N-related epitopes recognized by three new monoclonal antibodies. Glycoconjugate J. 7:225.
18. Jaskiewicz, E., J. J. Moulds, K. Kraemer, A. S. Goldstein, and E. Lisowska. 1990. Characterization of the epitope recognized by a monoclonal antibody highly specific for blood group M antigen. Transfusion 30:230.
19. g antigen: an example of modulation of antigenic properties of peptide by its glycosylation. Blood 84:2340.
20. Rubocki, R., and F. Milgrom. 1986. Reactions of murine monoclonal antibodies to blood group MN antigens. Vox Sang. 51:217.
21. Wasniowska, K., M. Duk, I. Steuden, M. Czerwinski, A. Wiedlocha, and E. Lisowska. 1988. Two monoclonal antibodies recognizing different epitopes of blood group N antigen. Arch. Immunol. Ther. Exp. 36:623.
22. Blackall, D. P., M. Ugorski, P. Pählsson, S. H. Shakin-Eshleman, and S. L. Spitalnik. 1994. A molecular biological approach to study the fine specificity of antibodies directed to the MN human blood group antigens. J. Immunol 152:2241.
23. Duk, M., U. Sticher, R. Brossmer, and E. Lisowska. 1994. The differences in significance of α2,3Gal-linked and α2,6GaINAc-linked sialic acid residues in blood group M-and N-related epitopes recognized by various monoclonal antibodies. Glycobiology 4:175.
24. H gene usage by murine hybridomas directed against the human N, but not M, blood group antigen. Mol. Immunol. 31:279.
25. Czerwinski, M., D. L. Siegel, J. S. Moore, P. F. Spitalnik, and S. L. Spitalnik. 1995. Construction of bacteriophage expressing mouse monoclonal Fab fragments directed against the human MN glycophorin blood group antigens. Transfusion 35:137.
26. Fraker, P. J., and J. C. Speck. 1978. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycoluril. Biochem. Biophys. Res. Commun. 80:849.
27. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248.
28. Hernando, J. J., S. von Kleist, and F. Grunert. 1994. A repertoire of monoclonal antibodies reveals extensive epitope heterogeneity in CEA purified from neoplasms originating from different organs. Int. J. Cancer 56:655.
29. Barbas, C. F., and R. A. Lerner. 1991. Combinatorial immunoglobulin libraries on the surface of phage (Phabs): rapid selection of antigen-specific Fabs. Methods 2:119.
30. Barbas, C. F., and D. R. Burton. 1994. Cold Spring Harbor Laboratory Course on Monoclonal Antibodies from Combinatorial Libraries: Course Materials. Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
31. Chomczynski, P., and N Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156.
32. Kang, A. S., Jones, T. M., and D. R. Burton. 1991. Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries. Proc. Natl. Acad. Sci. USA 88:11120.
33. Kettleborough, C. A., J. Saldanha, K. H. Ansell, and M. M. Bendig. 1993. Optimization of primers for cloning of mouse immunoglobulin genes using the polymerase chain reaction. Eur. J. Immunol. 23:206.
34. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
35. Wojczyk, B. S., M. E. Czerwinski, M. M. Stwora-Wojczyk, D. L. Siegel, W. H. Wunner, and S. L. Spitalnik. 1996. Purification of a secreted recombinant form of rabies virus glycoprotein: comparison of two affinity tags. Protein Exp. Purif. 7:183.
36. Harrison, J. L., S. C. Williams. G. Winter, and A. Nissim. 1995. Screening of phage antibody libraries. Methods Enzymol. 267:83.
37. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the dead of bacteriophage T4. Nature 227:680.
38. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350.
39. Hoessli, D., J. Olander, and J. R. Little. 1974. Heterologous recombination between mouse myeloma 315 heavy chains and rabbit antibody light chains: structural and functional properties of the hybrid molecules. J. Immunol. 113:1024.
40. k gene classification by nucleic acid sequence similarity. Immunogenetics 30:475.
41. Caton, A. J., S. E. Stark, J. Kavaler, L. M. Staudt, D. Schwartz, and W. Gerhard. 1991. Many variable region genes are utilized in the antibody response of BALB/C mice to the influenza virus A/PR/8/34 hemagglutinin. J. Immunol. 147: 1675.
42. Ishioka, G. Y., A. G. Lamont, D. Thomson, N. Bulbow, F. C. A. Gaeta, A. Sette, and H. M. Grey. 1992. MHC interaction and T cell recognition of carbohydrates and glycopeptides. J. Immunol. 148:2446.
43. Harding, C. V., J. Kihlberg, M. Elofsson, G. Magnusson, and E. R. Unanue. 1993. Glycopeptides bind MHC molecules and elicit specific T cell responses. J. Immunol. 151:2419.
44. Mouritsen, S., M. Meldal, I. Christiansen-Brams, H. Elsner, and O. Werdelin. 1994. Attachment of oligosaccharides to peptide antigen profoundly affects binding to major histocompatibility complex class II molecules and peptide immunogenicity. Eur. J. Immunol. 24:1066.
45. Otvos, L., L. Urge, Z. Q. Xiang, G. R. Krivulka, L. Nagy, G. I. Szendrei, and H. C. J. Ertl. 1994. Glycosylation of synthetic T helper cell epitopic peptides influences their antigenic potency and conformation in a sugar location-specific manner. Biochim. Biophys. Acta 1224:68.
46. Otvos, L., G. R. Krivulka, L. Urge, G. I. Szendrei, L. Nagy, Z. Q. Xiang, and H. C. J. Ertl. 1995. Comparison of the effects of amino acid substitutions and β-N-vs. α-O-glycosylation on the T-cell stimulatory activity and conformation of an epitope on the rabies virus glycoprotein. Biochim. Biophys. Acta 1267:55.
47. Dudler, T., F. Altmann, J. M. Carballido, and K. Blaser. 1995. Carbohydrate-dependent, HLA class Il-restricted, human T cell response to the bee venom allergen phospholipase A2 in allergic patients. Eur. J. Immunol. 25:538.
48. Otvos, L., B. Cappelletto, I. Varga, J. D. Wade, Z. Q. Xiang, K. Kaiser, L. J. Stevens, and H. C. J. Ertl. 1996. The effects of post-translational side-chain modifications on the stimulatory activity, serum stability and conformation of synthetic peptides carrying T helper cell epitopes. Biochim. Biophys. Acta 1313: 11.
49. Michaelsson, E., J. Broddefalk, A. Engstrom, J. Kihlberg, and R. Holmdahl. 1996. Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class II-restricted, carbohydrate-specific T cells. Eur. J. Immunol. 26:1906.
50. b-binding peptides generates carbohydrate-specific, unrestricted cytotoxic T cells. Eur. J. Immunol. 26:544.
51. Haurum, J. S., L. Tan, G. Arsequell, P. Frodsham, A. C. Lellouch, P. A. H. Moss, R. A. Dwek, A. J. McMichael, and T. Elliott. 1995. Peptide anchor residue glycosylation: effect on class I major histocompatibility complex binding and cytotoxic T lymphocyte recognition. Eur. J. Immunol. 25:3270.
52. Jensen, T., L. Galli-Stampino, S. Mouritsen, K. Frische, S. Peters, M. Meldal, and O. Werdelin. 1996. T cell recognition of Tn-glycosylated peptide antigens. Eur. J. Immunol. 26:1342.
53. Telischi, M., O. Behzak, P. D. Issitt, and B. G. Pavone. 1976. Hemolytic disease of the newborn due to anti-N. Vox Sang. 31:109.
54. Holliman, S. M. 1989. The MN blood group system: distribution, serology, and genetics. In Blood Group Systems: MN and Gerbich, P. J. Unger and B. Laird-Fryer, eds. American Association of Blood Banks, Arlington, VA. p. 1.
55. Edelman, G. M., D. E. Olins, J. A. Gally, and N. D. Zinder. 1963. Reconstitution of immunologic activity by interaction of polypeptide chains of antibodies. J. Exp. Med. 50:753.
56. Bridges, S. H., and J. R. Little. 1971. Recovery of binding activity in reconstituted mouse myeloma proteins. Biochemistry 10:2525.
57. Clackson, T., H. R. Hoogenboom, A. D. Griffiths, and G. Winter. 1991. Making antibody fragments using phage display libraries. Nature 352:624.
58. Griffiths, A. D., S. C. Williams, O. Hartley, I. M. Tomlinson, P. Waterhouse, W. L. Crosby, R. E. Kontermann, P. T. Jones, N. M. Low, T. J. Allison, T. D. Prospero, H. R. Hoogenboom, A. Nissim, J. P. L. Cox, J. L. Harrison, M. Zaccolo, E. Gherardi, and G. Winter. 1994. Isolation of high affinity human antibodies directly from large synthetic repertoires. EMBO J. 13:3245.
59. Ohlin, M., H. Owman, M. Mach, and C. A. K. Borrebaeck. 1996. Light chain shuffling of a high affinity antibody results in a drift in epitope recognition. Mol. Immunol. 33:47.
60. Jaume, J. C., G. Costante, S. Portolano, S. M. McLachlan, and B. Rapoport. 1994. Recombinant thyroid peroxidase-specific autoantibodies. I. How diverse is the pool of heavy and light chains in immunoglobulin gene libraries constructed from thyroid tissue-infiltrating plasma cells? Endocrinology 134:16.
61. Collet, T. A., P. Roben, R. O'Kennedy, C. F. Barbas, D. R. Burton, and R. A. Lerner. 1992. A binary plasmid system for shuffling combinatorial antibody libraries. Proc. Natl. Acad. Sci. USA 89:10026.
62. k joining amino acids, and the unique H chain D region for the high affinity binding of an anti-phosphotyrosine antibody. J. Immunol. 150: 3389.
63. Ames, R. S., M. A. Tornetta, L. J. McMillan, K. F. Kaiser, S. D. Holmes, E. Appelbaum, D. M. Cusimano, T. W. Theisen, M. S. Gross, C. S. Jones, C. Silverman, T. G. Porter, R. M. Cook, D. Bennett. and I. M. Chaiken. 1995. Neutralizing murine monoclonal antibodies to human IL-5 isolated from hybridomas and a filamentous phage Fab display library. J. Immunol. 154:6355.
64. Barry, M. M., and J. S. Lee. 1993. Cloning and expression of an autoimmune DNA-binding single chain Fv: only the heavy chain is required for binding. Mol. Immunol. 30:833.
65. Ibrahim, S. M., M. Weigert, C. Basu, J. Erikson, and M. Z. Radic. 1995. Light chain contribution to specificity in anti-DNA antibodies. J. Immunol. 155:3223.
66. Radie, M. Z., M. A. Mascelli, E. J., H. Shan, and M. Weigert. 1991. Ig H and L chain contributions to autoimmune specificities. J. Immunol 146:176.
67. x from a phage display library. J. Immunol. 157:732.
68. Ward, E. S., D. Gussow, A. D. Griffiths, P. T. Jones, and G. Winter. 1989. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 341:544.
69. Brummell, D. A., V. P. Sharma, N. N. Anand, D. Bilous, G. Dubuc, J. Michniewicz, C. R. MacKenzie, J. Sadowska, B. W. Sigurskjold, B. Sinnott, N. M. Young, D. R. Bundle, and S. A. Narang. 1993. Probing the combining site of an anti-carbohydrate antibody by saturation-mutagenesis: role of the heavy-chain CDR3 residues. Biochemistry 32:1180.
70. Bundle, D. R., E. Eichler, M. A. J. Gidney, M. Meldal. A. Ragauskas, B. W. Sigurskjold, B. Sinnott, D. C. Watson, M. Yaguchi, and N. M. Young. 1994. Molecular recognition of a Salmonella trisaccharide epitope by monoclonal antibody Sel55-4. Biochemistry 33:5172.
71. Bundle, D. R., H. Baumann, J. R. Brisson, S. M. Gagne, A. Zdanov, and M. Cygler. 1994. Solution structure of a trisaccharide-antibody complex: comparison of NMR measurements with a crystal structure. Biochemistry 33:5183.
72. Cygler, M., D. R. Rose, and D. R. Bundle, 1991. Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. Science 253:442.
73. Jeffrey, P. D., J. Bajorath, C. Y. Chang, D. Yelton, I. Hellstrom, K. E. Hellstrom, and S. Sheriff. 1995. The x-ray structure of an anti-tumour antibody in complex with antigen. Nat. Struct. Biol. 2:466.
74. Griffiths, G. M., C. Berek, M. Kaartinen, and C. Milstein. 1984. Somatic mutation and the maturation of the immune response to 2-phenyl oxazolone. Nature 312: 271.
75. Berek, C., and C. Milstein. 1987. Mutational drift and repertoire shift in the maturation of the immune response. Immunol. Rev. 96:23.
76. k gene segments of A/J Ars-A antibodies: somatic recombination generates the essential arginine at the junction of the variable and joining regions. Proc. Natl. Acad. Sci. USA 84:1085.
77. k-1 variability subgroup. J. Immunol. 138:932.
78. k-1 light chains. Ann. Immunol. 135.-C163.